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Protein

Proteasome subunit beta type-1

Gene

PSMB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).3 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processHost-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-1169091 Activation of NF-kappaB in B cells
R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974 ER-Phagosome pathway
R-HSA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154 APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534 Vpu mediated degradation of CD4
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253 Degradation of beta-catenin by the destruction complex
R-HSA-202424 Downstream TCR signaling
R-HSA-211733 Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562 Regulation of ornithine decarboxylase (ODC)
R-HSA-382556 ABC-family proteins mediated transport
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870 Asymmetric localization of PCP proteins
R-HSA-4641257 Degradation of AXIN
R-HSA-4641258 Degradation of DVL
R-HSA-5358346 Hedgehog ligand biogenesis
R-HSA-5362768 Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-5658442 Regulation of RAS by GAPs
R-HSA-5668541 TNFR2 non-canonical NF-kB pathway
R-HSA-5676590 NIK-->noncanonical NF-kB signaling
R-HSA-5678895 Defective CFTR causes cystic fibrosis
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-6798695 Neutrophil degranulation
R-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949 Orc1 removal from chromatin
R-HSA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-HSA-69481 G2/M Checkpoints
R-HSA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPSiT01.986

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-1 (EC:3.4.25.11 Publication)
Alternative name(s):
Macropain subunit C5
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Proteasome gamma chain
Gene namesi
Name:PSMB1
Synonyms:PSC5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000008018.8
HGNCiHGNC:9537 PSMB1
MIMi602017 gene
neXtProtiNX_P20618

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5689
OpenTargetsiENSG00000008018
PharmGKBiPA33882

Chemistry databases

ChEMBLiCHEMBL4208
DrugBankiDB00188 Bortezomib
DB08889 Carfilzomib
GuidetoPHARMACOLOGYi2404

Polymorphism and mutation databases

BioMutaiPSMB1
DMDMi130853

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00002596231 – 281 PublicationAdd BLAST28
ChainiPRO_000014803029 – 241Proteasome subunit beta type-1Add BLAST213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Glycosylationi58O-linked (GlcNAc) serineBy similarity1
Modified residuei62PhosphoserineCombined sources1
Modified residuei68PhosphoserineCombined sources1
Modified residuei150PhosphotyrosineBy similarity1
Modified residuei162PhosphoserineCombined sources1
Modified residuei204N6-acetyllysineCombined sources1
Glycosylationi209O-linked (GlcNAc) serineBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP20618
MaxQBiP20618
PaxDbiP20618
PeptideAtlasiP20618
PRIDEiP20618
TopDownProteomicsiP20618

2D gel databases

REPRODUCTION-2DPAGEiIPI00025019
UCD-2DPAGEiP20618

PTM databases

iPTMnetiP20618
PhosphoSitePlusiP20618
SwissPalmiP20618

Expressioni

Gene expression databases

BgeeiENSG00000008018
CleanExiHS_PSMB1
ExpressionAtlasiP20618 baseline and differential
GenevisibleiP20618 HS

Organism-specific databases

HPAiCAB033911
HPA029635
HPA029637

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. Interacts with SERPINB2 (PubMed:14732874). Interacts with HIV-1 TAT protein (PubMed:14550573).7 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111662, 131 interactors
CORUMiP20618
DIPiDIP-31193N
IntActiP20618, 81 interactors
MINTiP20618
STRINGi9606.ENSP00000262193

Chemistry databases

BindingDBiP20618

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 44Combined sources6
Beta strandi49 – 54Combined sources6
Beta strandi57 – 59Combined sources3
Beta strandi62 – 66Combined sources5
Beta strandi71 – 75Combined sources5
Beta strandi78 – 84Combined sources7
Helixi86 – 107Combined sources22
Helixi113 – 126Combined sources14
Turni127 – 129Combined sources3
Beta strandi134 – 141Combined sources8
Beta strandi147 – 152Combined sources6
Beta strandi158 – 167Combined sources10
Helixi170 – 180Combined sources11
Helixi196 – 213Combined sources18
Beta strandi214 – 217Combined sources4
Beta strandi219 – 227Combined sources9
Beta strandi230 – 237Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.601/M29-241[»]
4R67X-ray2.891/M/a/o29-241[»]
5A0Qelectron microscopy3.50M/a29-241[»]
5GJQelectron microscopy4.50f/t1-241[»]
5GJRelectron microscopy3.50f/t1-241[»]
5L4Gelectron microscopy4.021/U1-241[»]
5L5BX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5DX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5EX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5FX-ray2.50L/Z124-138[»]
L/Z145-160[»]
5L5HX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5IX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5JX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5OX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5PX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5QX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5RX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5SX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5TX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5UX-ray2.60L/Z124-138[»]
L/Z145-160[»]
5L5VX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L5WX-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L5XX-ray2.90L/Z124-138[»]
L/Z145-160[»]
5L5YX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L5ZX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L60X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L61X-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L62X-ray2.80L/Z124-138[»]
L/Z145-160[»]
5L63X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5L64X-ray2.70L/Z124-138[»]
L/Z145-160[»]
5LE5X-ray1.80L/Z29-241[»]
5LEXX-ray2.20L/Z29-241[»]
5LEYX-ray1.90L/Z29-241[»]
5LEZX-ray2.19L/Z29-241[»]
5LF0X-ray2.41L/Z29-241[»]
5LF1X-ray2.00L/Z29-241[»]
5LF3X-ray2.10L/Z29-241[»]
5LF4X-ray1.99L/Z29-241[»]
5LF6X-ray2.07L/Z29-241[»]
5LF7X-ray2.00L/Z29-241[»]
5LN3electron microscopy6.8061-241[»]
5M2BX-ray2.70L/Z124-138[»]
L/Z145-160[»]
5M32electron microscopy3.80L/Z1-241[»]
5T0Celectron microscopy3.80AS/BS2-241[»]
5T0Gelectron microscopy4.40S2-241[»]
5T0Helectron microscopy6.80S2-241[»]
5T0Ielectron microscopy8.00S2-241[»]
5T0Jelectron microscopy8.00S2-241[»]
6AVOelectron microscopy3.80S/X29-241[»]
ProteinModelPortaliP20618
SMRiP20618
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0179 Eukaryota
COG0638 LUCA
GeneTreeiENSGT00550000075035
HOGENOMiHOG000091081
HOVERGENiHBG000961
InParanoidiP20618
KOiK02732
OMAiEHRFNPY
OrthoDBiEOG091G0FUK
PhylomeDBiP20618
TreeFamiTF106218

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR035202 Proteasome_beta1
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF59 PTHR11599:SF59, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI
60 70 80 90 100
VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL
110 120 130 140 150
KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY
160 170 180 190 200
SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM
210 220 230 240
RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK D
Length:241
Mass (Da):26,489
Last modified:May 1, 1992 - v2
Checksum:iAE8FC42799F39157
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05154711P → A1 PublicationCorresponds to variant dbSNP:rs12717Ensembl.1
Natural variantiVAR_051548208I → N. Corresponds to variant dbSNP:rs10541Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00761 mRNA Translation: BAA00658.1
BT019720 mRNA Translation: AAV38525.1
AB451312 mRNA Translation: BAG70126.1
AB451442 mRNA Translation: BAG70256.1
AL031259 Genomic DNA No translation available.
BC000508 mRNA Translation: AAH00508.1
BC020807 mRNA Translation: AAH20807.1
CCDSiCCDS34577.1
PIRiS15973 SNHUC5
RefSeqiNP_002784.1, NM_002793.3
UniGeneiHs.352768

Genome annotation databases

EnsembliENST00000262193; ENSP00000262193; ENSG00000008018
GeneIDi5689
KEGGihsa:5689
UCSCiuc011ehe.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSB1_HUMAN
AccessioniPrimary (citable) accession number: P20618
Secondary accession number(s): B5BU76, Q9BWA8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 1, 1992
Last modified: May 23, 2018
This is version 199 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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